By Timo Weide, Armin Modlinger, Horst Kessler (auth.), Thomas Peters (eds.)
From the reviews:
"Bioactive Conformation I comprises 8 chapters on particularly varied issues in the topic of the sequence. … will probably be crucial examining for any researcher operating in any region that includes binding of a substance to a protein." (T. B. Grindley, magazine of the yank Chemical Society, Vol. a hundred thirty (2), 2008)
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Additional resources for Bioactive Conformation I
Kessler H, Kutscher B, Kerssebaum R, Klein A, Lautz J, Obermeier R, Muellner H, Van Gunsteren WF, Boelens R, Kaptein R (1985) In: Peptides: Structure and Function, Proc 9th Am Pept Symp, p 83 79. Kessler H, Kutscher B (1985) Tetrahedron Lett 26:177 80. Fujii N, Oishi S, Hiramatsu K, Araki T, Ueda S, Tamamura H, Otaka A, Kusano S, Terakubo S, Nakashima H, Broach JA, Trent JO, Wang ZX, Peiper SC (2003) Angew Chem Int Ed 42:3251 81. Tamamura H, Mizumoto M, Hiramatsu K, Kusano S, Terakubo S, Yamamoto N, Trent JO, Wang ZX, Peiper SC, Nakashima H, Otaka A, Fujii N (2004) Org Biomol Chem 2:1255 82.
Fig. 13 A schematic illustration of a cyclic parent pentapeptide with one d-amino acid and its inverso and retro–inverso isomers: the case of cyclo(-RGDfV-). The peptide sequence is shown clockwise from N- to C-terminus  Fig. 14 Comparison of the conformation of the parent peptide cyclo(-RGDfV-) and its retro-enantiomer-turn analogue. An almost identical side chain topology is found although the amide bonds are reversed. There is a loss of activity in the retro–inverso-turn analogue  20 T.
Due to the shifted hydrogen bond pattern and the different spatial structure compared to its parent compound, these conformational changes often result in a dramatic decrease of activity. The replacement of CONH with NHCO resulted in different bond angles and bond lengths . To delineate the different hydrogen bonding pattern restrictions a comparison of the retro–inverso peptide analogue to cyclo(-RGDfV-) is suggested to be most illustrative . The retro–inverso isomer cyclo(-vFdGr) contains only one l-amino acid (besides Gly) and we expected a βII-conformation about Phe-d-Asp.